Physicochemical properties and stability of anthralin in model systems and human skin.

Physicochemical properties and stability of anthralin in model systems and human skin.
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蒽林在模型系统和人体皮肤中的理化性质和稳定性。

DOI:
10.1111/1523-1747.ep12530811
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发表时间:
1983
期刊:
The Journal of investigative dermatology
影响因子:
--
通讯作者:
R. Santus
R. Santus
中科院分区:
--
文献类型:
--
作者:
T. S. Melo;L. Dubertret;P. Prognon;A. Gond;G. Mahuzier;R. Santus

文献摘要

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蒽林,一种有效的抗银屑病剂,的物理化学性质和稳定性,已在模型系统中进行了研究,通过光学吸收和荧光光谱,并通过气相色谱-质谱联用。本文对蒽林及其氧化产物1,8-二羟基蒽醌和1,8 - 1 ',8'-四羟基二蒽酮进行了系统的研究。蒽林和1,8-二羟基蒽醌显示出容易与人血清白蛋白结合而不与DNA结合。与白蛋白结合的蒽林容易氧化,产生相当稳定的1,8-二羟基蒽醌。这些结果与完整的整个人表皮和吸疱液所获得的结果相关,表明在前一种情况下,蒽林与蛋白质结合,如吸收和荧光光谱所示。气相色谱-质谱联用分析可以很容易地检测到蒽林和1,8-二羟基蒽醌在吸入水泡液掺杂蒽林,但不是在吸入水泡后,局部应用于正常人体皮肤。
The physico-chemical properties and the stability of anthralin, a potent antipsoriatic agent, has been investigated in model systems by optical absorption and fluorescence spectroscopy and by gas chromatography coupled to mass spectrometry. Systematic studies were carried out on anthralin and its oxidation products (1,8-dihydroxyanthraquinone and 1,8-1',8'-tetrahydroxydianthron). Anthralin and 1,8-dihydroxyanthraquinone are shown to readily bind to human serum albumin and not to DNA. Anthralin bound to albumin readily oxidizes, yielding the 1,8-dihydroxyanthraquinone which is fairly stable. These results are correlated with those obtained with intact whole human epidermis and suction blister fluid showing that, in the former case, anthralin binds to protein as suggested by absorption and fluorescence spectroscopies. Gas chromatography-mass spectrometry analysis makes it easy to detect anthralin and 1,8-dihydroxyanthraquinone in suction blister fluid doped with anthralin but not in suction blister obtained after topical application on normal human skin.